The Folding Pathway of a Single Domain in a Multidomain Protein is not Affected by Its Neighbouring Domain

Journal of Molecular Biology

Volumn 378, Issue 2, 2008, Pages 297-301

  Batey, Sarah ^a   Clarke, Jane ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

cooperativity; domain domain interactions; multidomain proteins; protein folding mechanisms; spectrin

Indexed keywords

FODRIN;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

EID: 41249094534     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.032     Document Type: Article

References (24)

1. Teichmann S.A., Chothia C., and Gerstein M. Advances in structural genomics. Curr. Opin. Struct. Biol. 9 (1999) 390-399
2. Batey S., and Clarke J. Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains. Proc. Natl Acad. Sci. USA 103 (2006) 18113-18118
3. Batey S., Randles L.G., Steward A., and Clarke J. Cooperative folding in a multi-domain protein. J. Mol. Biol. 349 (2005) 1045-1059
4. Batey S., Scott K.A., and Clarke J. Complex folding kinetics of a multidomain protein. Biophys. J. 90 (2006) 2120-2130
5. Jager M., Gehrig P., and Pluckthun A. The scFv fragment of the antibody hu4D5-8: evidence for early premature domain interaction in refolding. J. Mol. Biol. 305 (2001) 1111-1129
6. Osvath S., Kohler G., Zavodszky P., and Fidy J. Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase. Protein Sci. 14 (2005) 1609-1616
7. Politou A.S., Gautel M., Improta S., Vangelista L., and Pastore A. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255 (1996) 604-616
8. Robertsson J., Petzold K., Lofvenberg L., and Backman L. Folding of spectrin's SH3 domain in the presence of spectrin repeats. Cell. Mol. Biol. Lett. 10 (2005) 595-612
9. Rothlisberger D., Honegger A., and Pluckthun A. Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability. J. Mol. Biol. 347 (2005) 773-789
10. Scott K.A., Steward A., Fowler S.B., and Clarke J. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315 (2002) 819-829
11. Steward A., Adhya S., and Clarke J. Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. J. Mol. Biol. 318 (2002) 935-940
12. Wenk M., Jaenicke R., and Mayr E.M. Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438 (1998) 127-130
13. Han J.H., Batey S., Nickson A.A., Teichmann S.A., and Clarke J. The folding and evolution of multidomain proteins. Nat. Rev. Mol. Cell Biol. 8 (2007) 319-330
14. Kusunoki H., Minasov G., Macdonald R.I., and Mondragon A. Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin. J. Mol. Biol. 344 (2004) 495-511
15. Macdonald R.I., and Pozharski E.V. Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry 40 (2001) 3974-3984
16. MacDonald R.I., and Cummings J.A. Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer. Proc. Natl Acad. Sci. USA 101 (2004) 1502-1507
17. Randles L.G., Batey S., Steward A., and Clarke J. Distinguishing specific and non-specific inter-domain interactions in multidomain proteins. Biophys. J. 94 (2008) 622-628
18. Scott K.A., Batey S., Hooton K.A., and Clarke J. The folding of spectrin domains: I. Wild-type domains have the same stability but very different kinetic properties. J. Mol. Biol. 344 (2004) 195-205
19. Scott K.A., Randles L.G., and Clarke J. The folding of spectrin domains: II. Phi-value analysis of R16. J. Mol. Biol. 344 (2004) 207-221
20. Scott K.A., Randles L.G., Moran S.J., Daggett V., and Clarke J. The folding pathway of spectrin R17 from experiment and simulation: using experimentally validated MD simulations to characterize states hinted at by experiment. J. Mol. Biol. 359 (2006) 159-173
21. Scott K.A., and Clarke J. Spectrin R16: broad energy barrier or sequential transition states?. Protein Sci. 14 (2005) 1617-1629
22. Sanchez I.E., and Kiefhaber T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325 (2003) 367-376
23. Bachmann A., and Kiefhaber T. Apparent two-state tendamistat folding is a sequential process along a defined route. J. Mol. Biol. 306 (2001) 375-386
24. Minton A.P. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10 (2000) 34-39